Search

Your search keyword '"Hamilton, Susan"' showing total 454 results
Start Over Author "Hamilton, Susan" Search Limiters Available in Library Collection
454 results on '"Hamilton, Susan"'

6. Accounting for identity : becoming a chartered accountant

Author

Hamilton, Susan Elizabeth and Edwards, Richard

Subjects
657.0711, Accounting education, professional identity, interpretivist approach, metaphors, Accountants Education Scotland, Accounting Study and teaching, Accounting Students Identity
Abstract

This is a qualitative study which draws on the interpretivist tradition to research the processes by which Chartered Accountant (CA) students begin to develop their sense of professional identity. The thesis draws upon recent research on identity in early professional learning, in particular the aspects of becoming and belonging through which people enter into a community of practice. The purpose of the research is to understand the developing professional identity of students of the Institute of Chartered Accountants of Scotland (CA Students). In order to develop this understanding, data gathered at a number of focus groups at which CA Students were the participants, have been analysed. The transcripts from these focus groups are the primary source of data. This was analysed thematically and metaphorically in order to explore the senses that CA Students were making of their own entry into the accountancy profession. The analysis was used inductively to produce a resulting theory which has developed as a Professional Identity Map of the CA Student (PIMCAS). It elaborates the processes that impact on the developing professional identity of the CA Student. The findings of the research illuminate the processes by which CA Students become and belong, in particular marking the influence of the Training Firm and the Individual Values of the CA Student. The notions of becoming and belonging underpin the stories the CA Students tell of how they understand their developing professional identity. The practical implication of the results of this research for the future training of CAs is finally explored.

Published
2007

11. Adaptive thermogenesis enhances the life-threatening response to heat in mice with an Ryr1 mutation

Author

Wang, Hui J., Lee, Chang Seok, Yee, Rachel Sue Zhen, Groom, Linda, Friedman, Inbar, Babcock, Lyle, Georgiou, Dimitra K., Hong, Jin, Hanna, Amy D., Recio, Joseph, Choi, Jong Min, Chang, Ting, Agha, Nadia H., Romero, Jonathan, Sarkar, Poonam, Voermans, Nicol, Gaber, M. Waleed, Jung, Sung Yun, Baker, Matthew L., Pautler, Robia G., Dirksen, Robert T., Riazi, Sheila, and Hamilton, Susan L.

Published
2020
Full Text
View/download PDF

31. Crystal structure of dimeric cardiac L-type calcium channel regulatory domains bridged by [Ca.sup.2+] x calmodulins

Author

Fallon, Jennifer L., Baker, Mariah R., Xiong, Liangwen, Loy, Ryan E., Yang, Guojun, Dirksen, Robert T., Hamilton, Susan L., and Quiocho, Florante A.

Subjects
Calcium channels -- Structure, Calcium channels -- Research, Calcium channels -- Economic policy, Calmodulin -- Research, Calmodulin -- Structure, Calcium-binding proteins -- Analysis, Crystals -- Structure, Crystals -- Analysis, Science and technology
Abstract

Voltage-dependent calcium channels (Car) open in response to changes in membrane potential, but their activity is modulated by [Ca.sup.2+] binding to calmodulin (CAM). Structural studies of this family of channels have focused on CaM bound to the IQ motif; however, the minimal differences between structures cannot adequately describe CaM's role in the regulation of these channels. We report a unique crystal structure of a 77-residue fragment of the [Ca.sub.v]1.2 [[alpha].sub.1] subunit carboxyl terminus, which includes a tandem of the pre-IQ and IQ domains, in complex with [Ca.sup.2+].CaM in 2 distinct binding modes. The structure of the [Ca.sub.v]1.2 fragment is an unusual dimer of 2 coiled-coiled pre-IQ regions bridged by 2 [Ca.sup.2+].CaMs interacting with the pre-IQ regions and a canonical [Ca.sub.v]1-IQ-[Ca.sup.2+]-CaM complex. Native [Ca.sub.v]1.2 channels are shown to be a mixture of monomers/dimers and a point mutation in the pre-IQ region predicted to abolish the coiled-coil structure significantly reduces [Ca.sup.2+]-dependent inactivation of heterologously expressed [Ca.sub.v]1.2 channels. structure | function | voltage-gated calcium channel

Published
2009

33. The skeletal muscle [Ca.sup.2+] release channel has an oxidoreductase-like domain

Author

Baker, Matthew L., Serysheva, Irina I., Sencer, Serap, Wu, Yili, Ludtke, Steven J., Jiang, Wen, Hamilton, Susan L., and Chiu, Wah

Subjects
Striated muscle -- Physiological aspects, Calcium channels -- Physiological aspects, Muscle proteins -- Physiological aspects, Structure-activity relationships (Biochemistry) -- Analysis, Science and technology
Abstract

We used a combination of bioinformatics, electron cryomicroscopy, and biochemical techniques to identify an oxidoreductase-like domain in the skeletal muscle [Ca.sup.2+] release channel protein (RyR1). The initial prediction was derived from sequence-based fold recognition for the N-terminal region (41-420) of RyR1. The putative domain was computationally localized to the clamp domain in the cytoplasmic region of a 22[Angstrom] structure of RyR1. This localization was subsequently confirmed by difference imaging with a sequence specific antibody. Consistent with the prediction of an oxidoreductase domain, RyR1 binds [[sup.3]H]NA[D.sup.+], supporting a model in which RyR1 has a oxidoreductase-like domain that could function as a type of redox sensor.

Published
2002

35. Cell-Free DNA in the Investigation of Miscarriage

Author

Colley, Emily, primary, Devall, Adam J., additional, Williams, Helen, additional, Hamilton, Susan, additional, Smith, Paul, additional, Morgan, Neil V., additional, Quenby, Siobhan, additional, Coomarasamy, Arri, additional, and Allen, Stephanie, additional

Published
2020
Full Text
View/download PDF

37. Assignment of muscarinic receptor subtypes mediating G-protein modulation of Ca2+ channels by using knockout mice

Author

Shapiro, Mark S., Loose, Michael D., Hamilton, Susan E., Nathanson, Neil M., Gomeza, Jesus, Wess, Jurgen, and Hille, Bertil

Subjects
Calcium channels -- Research, G proteins -- Research, Muscarinic receptors -- Research, Science and technology
Abstract

There are five known subtypes of muscarinic receptors ([M.sub.1]-[M.sub.5]). We have used knockout mice lacking the [M.sub.1], [M.sub.2], or [M.sub.4] receptors to determine which subtypes mediate modulation of voltage-gated [Ca.sup.2+] channels in mouse sympathetic neurons. Muscarinic agonists modulate N- and L-type [Ca.sup.2+] channels in these neurons through two distinct G-protein-mediated mechanisms. One pathway is fast and membrane-delimited and inhibits N- and P/Q-type channels by shifting their activation to more depolarized potentials. The other is slow and voltage-independent and uses a diffusible cytoplasmic messenger to inhibit both [Ca.sup.2+] channel types. Using patch-clamp methods on acutely dissociated sympathetic neurons, we isolated each pathway by pharmacological and kinetic means and found that each one is nearly absent in a particular knockout mouse. The fast and voltage-dependent pathway is lacking in the [M.sub.2] receptor knockout mice; the slow and voltage-independent pathway is absent from the [M.sub.1] receptor knockout mice; and neither pathway is affected in the [M.sub.4] receptor knockout mice. The knockout effects are clean and are apparently not accompanied by compensatory changes in other muscarinic receptors.

Published
1999

38. Prenatal exome sequencing analysis in fetal structural anomalies detected by ultrasonography (PAGE): a cohort study

Author

Lord, Jenny, McMullan, Dominic, Eberhardt, Ruth, Rinck, Gabriele, Hamilton, Susan, Quinlan-Jones, Elizabeth, Prigmore, Elena, Keelagher, Rebecca, Best, Sunayna, Carey, Georgina, Kilby, Mark, Chitty, Lyn, Hurles, Matthew, Maher, ER, and Apollo - University of Cambridge Repository

Subjects
Male, Parents, DNA Copy Number Variations, Perinatal Death, Infant, Newborn, Abnormal Karyotype, Stillbirth, Congenital Abnormalities, Abortion, Spontaneous, Fetal Development, Fetus, Pregnancy, Exome Sequencing, Humans, Female, Prospective Studies, Nuchal Translucency Measurement, Live Birth, Abortion, Eugenic
Abstract

Background: Fetal structural anomalies, which are detected by ultrasonography, have a range of genetic causes, including chromosomal aneuploidy, copy number variations (CNVs; which are detectable by chromosomal microarrays), and pathogenic sequence variants in developmental genes. Testing for aneuploidy and CNVs is routine during the investigation of fetal structural anomalies, but there is little information on the clinical usefulness of genome-wide next-generation sequencing in the prenatal setting. We therefore aimed to evaluate the proportion of fetuses with structural abnormalities that had identifiable variants in genes associated with developmental disorders when assessed with whole-exome sequencing (WES). Methods: In this prospective cohort study, two groups in Birmingham and London recruited patients from 34 fetal medicine units in England and Scotland. We used whole-exome sequencing (WES) to evaluate the presence of genetic variants in developmental disorder genes (diagnostic genetic variants) in a cohort of fetuses with structural anomalies and samples from their parents, after exclusion of aneuploidy and large CNVs. Women were eligible for inclusion if they were undergoing invasive testing for identified nuchal translucency or structural anomalies in their fetus, as detected by ultrasound after 11 weeks of gestation. The partners of these women also had to consent to participate. Sequencing results were interpreted with a targeted virtual gene panel for developmental disorders that comprised 1628 genes. Genetic results related to fetal structural anomaly phenotypes were then validated and reported postnatally. The primary endpoint, which was assessed in all fetuses, was the detection of diagnostic genetic variants considered to have caused the fetal developmental anomaly. Findings: The cohort was recruited between Oct 22, 2014, and June 29, 2017, and clinical data were collected until March 31, 2018. After exclusion of fetuses with aneuploidy and CNVs, 610 fetuses with structural anomalies and 1202 matched parental samples (analysed as 596 fetus-parental trios, including two sets of twins, and 14 fetus-parent dyads) were analysed by WES. After bioinformatic filtering and prioritisation according to allele frequency and effect on protein and inheritance pattern, 321 genetic variants (representing 255 potential diagnoses) were selected as potentially pathogenic genetic variants (diagnostic genetic variants), and these variants were reviewed by a multidisciplinary clinical review panel. A diagnostic genetic variant was identified in 52 (8·5%; 95% CI 6·4–11·0) of 610 fetuses assessed and an additional 24 (3·9%) fetuses had a variant of uncertain significance that had potential clinical usefulness. Detection of diagnostic genetic variants enabled us to distinguish between syndromic and non-syndromic fetal anomalies (eg, congenital heart disease only vs a syndrome with congenital heart disease and learning disability). Diagnostic genetic variants were present in 22 (15·4%) of 143 fetuses with multisystem anomalies (ie, more than one fetal structural anomaly), nine (11·1%) of 81 fetuses with cardiac anomalies, and ten (15·4%) of 65 fetuses with skeletal anomalies; these phenotypes were most commonly associated with diagnostic variants. However, diagnostic genetic variants were least common in fetuses with isolated increased nuchal translucency (≥4·0 mm) in the first trimester (in three [3·2%] of 93 fetuses). Interpretation: WES facilitates genetic diagnosis of fetal structural anomalies, which enables more accurate predictions of fetal prognosis and risk of recurrence in future pregnancies. However, the overall detection of diagnostic genetic variants in a prospectively ascertained cohort with a broad range of fetal structural anomalies is lower than that suggested by previous smaller-scale studies of fewer phenotypes. WES improved the identification of genetic disorders in fetuses with structural abnormalities; however, before clinical implementation, careful consideration should be given to case selection to maximise clinical usefulness.

Published
2019

39. TRPV1 variants impair intracellular Ca2+ signaling and may confer susceptibility to malignant hyperthermia

Author

Lotteau, Sabine, Ducreux, Sylvie, Dubois, Charlotte, Monnier, Nicole, Hanna, Amy, Gkika, Dimitra, Romestaing, Caroline, Noyer, Lucile, Flourakis, Matthieu, Tessier, Nolwenn, AL-MAWLA, Ribal, Chouabe, Christophe, Lefai, Etienne, Lunardi, Joël, Hamilton, Susan, Fauré, Julien, Prevarskaya, Natalia, Vanden Abeele, Fabien, and Van Coppenolle, Fabien

Subjects
TRP channel, TRPV1, calcium, hereditary disease, malignant hyperthermia, hyperthermie maligne, souris, maladie héréditaire
Abstract

Purpose: Malignant hyperthermia (MH) is a pharmacogenetic disorder arising from uncontrolled muscle calcium release due to an abnormality in the sarcoplasmic reticulum (SR) calcium-release mechanism triggered by halogenated inhalational anesthetics. However, the molecular mechanisms involved are still incomplete. Methods: We aimed to identify transient receptor potential vanilloid 1 (TRPV1) variants within the entire coding sequence in patients who developed sensitivity to MH of unknown etiology. In vitro and in vivo functional studies were performed in heterologous expression system, trpv1(-/-) mice, and a murine model of human MH. Results: We identified TRPV1 variants in two patients and their heterologous expression in muscles of trpv1-/- mice strongly enhanced calcium release from SR upon halogenated anesthetic stimulation, suggesting they could be responsible for the MH phenotype. We confirmed the in vivo significance by using mice with a knock-in mutation (Y524S) in the type I ryanodine receptor (Ryr1), a mutation analogous to the Y522S mutation associated with MH in humans. We showed that the TRPV1 antagonist capsazepine slows the heat-induced hypermetabolic response in this model. Conclusion: We propose that TRPV1 contributes to MH and could represent an actionable therapeutic target for prevention of the pathology and also be responsible for MH sensitivity when mutated.

Published
2019

40. TRPV1 variants impair intracellular Ca2+ signaling and may confer susceptibility to malignant hyperthermia

Author

Vanden Abeele, Fabien, Lotteau, Sabine, Ducreux, Sylvie, Dubois, charlotte, Monnier, Nicole, Amy, Hanna, Gkika, Dimitra, Romestaing, Caroline, Lucile, Noyer, Flourakis, Matthieu, Tessier, Nolwenn, Al-Mawla, Ribal, Chouabe, Christophe, Lefai, Etienne, Joël, Lunardi, Hamilton, Susan, Faure, Julien, Van Coppenolle, Fabien, Prevarskaya, Natalia, Laboratory of Excellence, Ion Channels Science and Therapeutics, Université de Lille, Sciences et Technologies, Cardiovasculaire, métabolisme, diabétologie et nutrition (CarMeN), Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM), School of Biomedical Sciences, University of Leeds, Biochimie et Genetique Moleculaire, CHU Grenoble, Department of Medicine and Department of Molecular Physiology & Biophysics, Baylor College of Medecine, Laboratoire de Physiologie Cellulaire : Canaux ioniques, inflammation et cancer - U1003 (PHYCELL), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Laboratoire d'Ecologie des Hydrosystèmes Naturels et Anthropisés (LEHNA), Université de Lyon-Université de Lyon-École Nationale des Travaux Publics de l'État (ENTPE)-Centre National de la Recherche Scientifique (CNRS), Grenoble Institut des Neurosciences (GIN), Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Universitaire [Grenoble] (CHU), LabEx ICST, Laboratoire d'excellence Canaux Ioniques d'Intérêt Thérapeutique, Equipe Labélisée par la Ligue Nationale Contre le Cancer, SIRIC ONCOLille, Université des Sciences et Technologies (Lille 1) (USTL), UMR 1397 CarMeN Cardiovasculaire, Métabolisme, Diabétologie et Nutrition. Centre de recherche Lyon-Grenoble-Auvergne-Rhône-Alpes, Institut National de la Recherche Agronomique (INRA), Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon, School of Biomedical Sciences, University of Ulster, Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Hospices Civils de Lyon (HCL), IBP, Laboratoire de Biochimie Génétique et Moléculaire, Department of Molecular Physiology and Biophysics, Baylor College of Medicine (BCM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-École Nationale des Travaux Publics de l'État (ENTPE), Centre National de la Recherche Scientifique (CNRS), École Nationale des Travaux Publics de l'État (ENTPE), GIN Grenoble Institut des Neurosciences, Université de Grenoble, French Ministere de l'Education Nationale, Institut National de la Sante et de la Recherche Medicale (Inserm), ANR program within the 'Investissements d'Avenir' [ANR-10-IBHU-0004], Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National de la Recherche Agronomique (INRA), Physiologie Cellulaire (PHYCEL) - U1003 (PHYCEL), Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Lille Nord de France (COMUE), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Joseph Fourier - Grenoble 1 (UJF)-Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Physiologie Cellulaire : Canaux ioniques, inflammation et cancer - U 1003 (PHYCELL), and ProdInra, Archive Ouverte

Subjects
Male, mice, [SDV]Life Sciences [q-bio], Gene Expression, TRPV Cation Channels, hereditary diseases, Hereditary disease, souris, maladie héréditaire, Article, Malignant hyperthermia, TRP channel, Animals, Homeostasis, Humans, Genetic Predisposition to Disease, Calcium Signaling, Gene Knock-In Techniques, Muscle, Skeletal, Anesthetics, hyperthermie maligne, [SDV] Life Sciences [q-bio], Mice, Inbred C57BL, TRPV1, Disease Models, Animal, HEK293 Cells, Female, Calcium, [SDE.BE]Environmental Sciences/Biodiversity and Ecology
Abstract

International audience; Purpose: Malignant hyperthermia (MH) is a pharmacogenetic disorder arising from uncontrolled muscle calcium release due to an abnormality in the sarcoplasmic reticulum (SR) calcium-release mechanism triggered by halogenated inhalational anesthetics. However, the molecular mechanisms involved are still incomplete.Methods: We aimed to identify transient receptor potential vanilloid 1 (TRPV1) variants within the entire coding sequence in patients who developed sensitivity to MH of unknown etiology. In vitro and in vivo functional studies were performed in heterologous expression system, trpv1−/− mice, and a murine model of human MH.Results: We identified TRPV1 variants in two patients and their heterologous expression in muscles of trpv1−/− mice strongly enhanced calcium release from SR upon halogenated anesthetic stimulation, suggesting they could be responsible for the MHphenotype. We confirmed the in vivo significance by using mice with a knock-in mutation (Y524S) in the type I ryanodine receptor (Ryr1), a mutation analogous to the Y522S mutation associated with MH in humans. We showed that the TRPV1 antagonist capsazepine slows the heat-induced hypermetabolic response in this model.Conclusion: We propose that TRPV1 contributes to MH and could represent an actionable therapeutic target for prevention of the pathology and also be responsible for MH sensitivity when mutated.Genetics in Medicine (2019) 21:441–450; https://doi.org/10.1038/s41436- 018-0066-9Keywords:TRP channel; TRPV1; Calcium; Hereditary disease; Malignant hyperthermia

Published
2019

43. Cardiac defects and altered ryanodine receptor function in mice lacking FKBP12

Author

Shou, Weinian, Aghdasi, Bahman, Armstrong, Dawna L., Guo, Qiuxia, Bao, Shideng, Charng, Min-Ji, Mathews, Lawrence M., Schneider, Michael D., Hamilton, Susan L., and Matzuk, Martin M.

Subjects
Cardiovascular receptors -- Research, Mice -- Physiological aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Mutant mice deficient in FKBP12, a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin, were generated using embryonic stem cell technology in order to define the functions of FKBP12 in vivo. Lipid bilayer experiments showed that lack of FKBP12 changes the single-channel properties of both cardiac RyR2 and skeletal RyR1. It is not possible for FKBP12.6 to functionally replace FKBP12. These defects could play a role in the cardiac phenotype in FKBP12-deficient mice.

Published
1998

49. A plasmid-based approach for the synthesis of a histidine biosynthetic intermediate

Author

Davisson, V. Jo, Deras, Ina L., Hamilton, Susan E., and Moore, Landon L.

Subjects
Histidine -- Research, Plasmids -- Usage, Biosynthesis -- Analysis, Biological sciences, Chemistry
Abstract

Bis-ribosyl nucleotide of purity which is suited for spectral analysis and biochemical studies is prepared through a histidine biosynthesis intermediate using a plasmid DNA construct. The recombinant DNA plasmid which controls overexpression of proteins is an enriched source of the first three enzymes in the histidine biosynthetic process.

Published
1994

Catalog

Books, media, physical & digital resources
See catalog results